Crystal structure of the Sth1 bromodomain from S.cerevisiae. Determined by X-ray diffraction at 2.71 Å resolution. Released 24 Jul 2019.
Explore 6MR4 in 3D Show helices and sheets RCSB PDB PDBe
6MR4 contains 45 α-helices and 12 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1252-1262 | 11 | |
| β-strand | 1266 | 1 | 1 |
| β-strand | 1273 | 1 | 1 |
| α-helix | 1276-1278 | 3 | |
| α-helix | 1281-1283 | 3 | |
| α-helix | 1288-1293 | 6 | |
| α-helix | 1300-1308 | 9 | |
| α-helix | 1315-1332 | 18 | |
| α-helix | 1334 | 1 | |
| α-helix | 1338-1356 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1252-1262 | 11 | |
| β-strand | 1266 | 1 | 2 |
| β-strand | 1273 | 1 | 2 |
| α-helix | 1276-1278 | 3 | |
| α-helix | 1281-1283 | 3 | |
| α-helix | 1288-1293 | 6 | |
| α-helix | 1300-1308 | 9 | |
| α-helix | 1315-1332 | 18 | |
| α-helix | 1334 | 1 | |
| α-helix | 1338-1355 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1252-1262 | 11 | |
| β-strand | 1266 | 1 | 3 |
| β-strand | 1273 | 1 | 3 |
| α-helix | 1276-1278 | 3 | |
| α-helix | 1281-1283 | 3 | |
| α-helix | 1288-1293 | 6 | |
| α-helix | 1300-1308 | 9 | |
| α-helix | 1315-1332 | 18 | |
| α-helix | 1338-1356 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear protein STH1/NPS1 | A, B, C, D, E, F | protein | 112 | Saccharomyces cerevisiae | P32597 (AlphaFold model) |
>6MR4_1 Nuclear protein STH1/NPS1 (chains A, B, C, D, E, F) SMGIFPTVEKLVEEMREQLDEVDSHPRTSIFEKLPSKRDYPDYFKVIEKPMAIDIILKNC KNGTYKTLEEVRQALQTMFENARFYNEEGSWVYVDADKLNEFTDEWFKEHSS
Substrate Affinity and Specificity of the ScSth1p Bromodomain Are Fine-Tuned for Versatile Histone Recognition. Blus, B.J., Hashimoto, H., Seo, H.S. et al. Structure (2019) 27:1460-1468.e3. DOI 10.1016/j.str.2019.06.009 · PubMed
Other PDB entries of the same protein (UniProt P32597 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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